Surfactant protein B inhibits secretory phospholipase A2 hydrolysis of surfactant phospholipids.

نویسندگان

  • R Duncan Hite
  • Bonnie L Grier
  • B Moseley Waite
  • Ruud A Veldhuizen
  • Fred Possmayer
  • Li-Juan Yao
  • Michael C Seeds
چکیده

Hydrolysis of surfactant phospholipids (PL) by secretory phospholipases A(2) (sPLA(2)) contributes to surfactant damage in inflammatory airway diseases such as acute lung injury/acute respiratory distress syndrome. We and others have reported that each sPLA(2) exhibits specificity in hydrolyzing different PLs in pulmonary surfactant and that the presence of hydrophilic surfactant protein A (SP-A) alters sPLA(2)-mediated hydrolysis. This report tests the hypothesis that hydrophobic SP-B also inhibits sPLA(2)-mediated surfactant hydrolysis. Three surfactant preparations were used containing varied amounts of SP-B and radiolabeled tracers of phosphatidylcholine (PC) or phosphatidylglycerol (PG): 1) washed ovine surfactant (OS) (pre- and postorganic extraction) compared with Survanta (protein poor), 2) Survanta supplemented with purified bovine SP-B (1-5%, wt/wt), and 3) a mixture of dipalmitoylphosphatidylcholine (DPPC), 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC), and 1-palmitoyl-2-oleoyl-phosphatidylglycerol (POPG) (DPPC:POPC:POPG, 40:40:20) prepared as vesicles and monomolecular films in the presence or absence of SP-B. Hydrolysis of PG and PC by Group IB sPLA(2) (PLA2G1A) was significantly lower in the extracted OS, which contains SP-B, compared with Survanta (P = 0.005), which is SP-B poor. Hydrolysis of PG and PC in nonextracted OS, which contains all SPs, was lower than both Survanta and extracted OS. When Survanta was supplemented with 1% SP-B, PG and PC hydrolysis by PLA2G1B was significantly lower (P < 0.001) than in Survanta alone. When supplemented into pure lipid vesicles and monomolecular films composed of PG and PC mixtures, SP-B also inhibited hydrolysis by both PLA2G1B and Group IIA sPLA2 (PLA2G2A). In films, PLA2G1B hydrolyzed surfactant PL monolayers at surface pressures ≤30 mN/m (P < 0.01), and SP-B lowered the surface pressure range at which hydrolysis can occur. These results suggest the hydrophobic SP, SP-B, protects alveolar surfactant PL from hydrolysis mediated by multiple sPLA(2) in both vesicles (alveolar subphase) and monomolecular films (air-liquid interface).

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منابع مشابه

Hydrolysis of surfactant-associated phosphatidylcholine by mammalian secretory phospholipases A2 R. DUNCAN HITE,1 MICHAEL C. SEEDS,1 RANDY B. JACINTO,1 R. BALASUBRAMANIAN,1 MOSELEY WAITE,2 AND DAVID BASS1

Hite, R. Duncan, Michael C. Seeds, Randy B. Jacinto, R. Balasubramanian, Moseley Waite, and David Bass. Hydrolysis of surfactant-associated phosphatidylcholine by mammalian secretory phospholipases A2. Am. J. Physiol. 275 (Lung Cell. Mol. Physiol. 19): L740–L747, 1998.—Hydrolysis of surfactant-associated phospholipids by secretory phospholipases A2 is an important potential mechanism for surfac...

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عنوان ژورنال:
  • American journal of physiology. Lung cellular and molecular physiology

دوره 302 2  شماره 

صفحات  -

تاریخ انتشار 2012